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Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy
α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same bindi...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9501389/ https://www.ncbi.nlm.nih.gov/pubmed/36136542 http://dx.doi.org/10.3390/toxins14090604 |
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author | Li, Yifang Tan, Hongxia Zhou, Hongyuan Guo, Ting Zhou, Ying Zhang, Yuhao Liu, Xiaozhu Ma, Liang |
author_facet | Li, Yifang Tan, Hongxia Zhou, Hongyuan Guo, Ting Zhou, Ying Zhang, Yuhao Liu, Xiaozhu Ma, Liang |
author_sort | Li, Yifang |
collection | PubMed |
description | α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same binding site as α-ZOL. Additionally, several studies reported that reducing the bound fraction of α-ZOL contributes to speeding up the elimination rate of α-ZOL to reduce its hazard to organs. Therefore, to explore the influence of a nutrition intervention with curcumin on α-ZOL effects, the competitive displacement of α-ZOL from HSA by curcumin was investigated using spectroscopic techniques, ultrafiltration techniques and HPLC methods. Results show that curcumin and α-ZOL share the same binding site (subdomain IIA) on HSA, and curcumin binds to HSA with a binding constant of 1.12 × 10(5) M(−1), which is higher than that of α-ZOL (3.98 × 10(4) M(−1)). Ultrafiltration studies demonstrated that curcumin could displace α-ZOL from HSA to reduce α-ZOL’s binding fraction. Synchronous fluorescence spectroscopy revealed that curcumin could reduce the hydrophobicity of the microenvironment of an HSA–α-ZOL complex. This study is of great significance for applying curcumin and other highly active foodborne components to interfere with the toxicokinetics of α-ZOL and reduce its risk of its exposure. |
format | Online Article Text |
id | pubmed-9501389 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-95013892022-09-24 Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy Li, Yifang Tan, Hongxia Zhou, Hongyuan Guo, Ting Zhou, Ying Zhang, Yuhao Liu, Xiaozhu Ma, Liang Toxins (Basel) Article α-zearalenol (α-ZOL) is a mycotoxin with a strong estrogen effect that affects the synthesis and secretion of sex hormones and is transported to target organs through human serum albumin (HSA). Additionally, it has been reported that curcumin can also bind to HSA with high affinity at the same binding site as α-ZOL. Additionally, several studies reported that reducing the bound fraction of α-ZOL contributes to speeding up the elimination rate of α-ZOL to reduce its hazard to organs. Therefore, to explore the influence of a nutrition intervention with curcumin on α-ZOL effects, the competitive displacement of α-ZOL from HSA by curcumin was investigated using spectroscopic techniques, ultrafiltration techniques and HPLC methods. Results show that curcumin and α-ZOL share the same binding site (subdomain IIA) on HSA, and curcumin binds to HSA with a binding constant of 1.12 × 10(5) M(−1), which is higher than that of α-ZOL (3.98 × 10(4) M(−1)). Ultrafiltration studies demonstrated that curcumin could displace α-ZOL from HSA to reduce α-ZOL’s binding fraction. Synchronous fluorescence spectroscopy revealed that curcumin could reduce the hydrophobicity of the microenvironment of an HSA–α-ZOL complex. This study is of great significance for applying curcumin and other highly active foodborne components to interfere with the toxicokinetics of α-ZOL and reduce its risk of its exposure. MDPI 2022-08-31 /pmc/articles/PMC9501389/ /pubmed/36136542 http://dx.doi.org/10.3390/toxins14090604 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Li, Yifang Tan, Hongxia Zhou, Hongyuan Guo, Ting Zhou, Ying Zhang, Yuhao Liu, Xiaozhu Ma, Liang Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy |
title | Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy |
title_full | Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy |
title_fullStr | Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy |
title_full_unstemmed | Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy |
title_short | Study of Competitive Displacement of Curcumin on α-zearalenol Binding to Human Serum Albumin Complex Using Fluorescence Spectroscopy |
title_sort | study of competitive displacement of curcumin on α-zearalenol binding to human serum albumin complex using fluorescence spectroscopy |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9501389/ https://www.ncbi.nlm.nih.gov/pubmed/36136542 http://dx.doi.org/10.3390/toxins14090604 |
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